Structure of PDB 6tmk Chain B2 Binding Site BS01

Receptor Information
>6tmk Chain B2 (length=479) Species: 507601 (Toxoplasma gondii GT1) [Search protein sequence] [Download receptor structure] [Download structure with residue number starting from 1] [View receptor structure]
TNHGRITQVIGAVVDVHFDEQLPPILNSLEVQGHTNRLVLEVAQHLGENT
VRTIAMDATEGLVRGQKVVDTGAPIQVPVGVETLGRIMNVIGEPVDECGP
VPAKKTYSIHRAAPLFADQSTEPGLLQTGIKVVDLLAPYAKGGKIGLFGG
AGVGKTVLIMELINNVANKHGGFSVFAGVGERTREGNDLYHEMMTTGVIK
RKKLEDGKFDFTGSKAALVYGQMNEPPGARARVALTALSVAEYFRDEQGQ
DVLLFIDNIYRFTQAGSEVSALLGRIPSAVGYQPTLATDLGQLQERITTT
KKGSITSVQAVYVPADDLTDPAPATTFAHLDATTVLSRQIAELGIYPAVD
PLDSTSRMLAPEIVGQEHYDTARATQKLLQDYKSLQDIIAILGMDELSEE
DKLVVSRARKIQRFLSQPFTVAEVFTGKPGRFVELPETIKSAQTILRGEC
DDLPEMAFYMCGGLEEVRSKAVKMAQEAA
Ligand information
Ligand IDADP
InChIInChI=1S/C10H15N5O10P2/c11-8-5-9(13-2-12-8)15(3-14-5)10-7(17)6(16)4(24-10)1-23-27(21,22)25-26(18,19)20/h2-4,6-7,10,16-17H,1H2,(H,21,22)(H2,11,12,13)(H2,18,19,20)/t4-,6-,7-,10-/m1/s1
InChIKeyXTWYTFMLZFPYCI-KQYNXXCUSA-N
SMILES
SoftwareSMILES
OpenEye OEToolkits 1.5.0c1nc(c2c(n1)n(cn2)[C@H]3[C@@H]([C@@H]([C@H](O3)CO[P@](=O)(O)OP(=O)(O)O)O)O)N
CACTVS 3.341Nc1ncnc2n(cnc12)[CH]3O[CH](CO[P](O)(=O)O[P](O)(O)=O)[CH](O)[CH]3O
ACDLabs 10.04O=P(O)(O)OP(=O)(O)OCC3OC(n2cnc1c(ncnc12)N)C(O)C3O
CACTVS 3.341Nc1ncnc2n(cnc12)[C@@H]3O[C@H](CO[P@@](O)(=O)O[P](O)(O)=O)[C@@H](O)[C@H]3O
OpenEye OEToolkits 1.5.0c1nc(c2c(n1)n(cn2)C3C(C(C(O3)COP(=O)(O)OP(=O)(O)O)O)O)N
FormulaC10 H15 N5 O10 P2
NameADENOSINE-5'-DIPHOSPHATE
ChEMBLCHEMBL14830
DrugBankDB16833
ZINCZINC000012360703
PDB chain6tmk Chain B2 Residue 601 [Download ligand structure] [Download structure with residue number starting from 1] [View ligand structure]
Receptor-Ligand Complex Structure
Global viewLocal viewStructure summary

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PDB6tmk ATP synthase hexamer assemblies shape cristae of Toxoplasma mitochondria.
Resolution2.9 Å
Binding residue
(original residue number in PDB)		A229 G230 G232 K233 T234 Y424 A500 F503
Binding residue
(residue number reindexed from 1)		A151 G152 G154 K155 T156 Y346 A422 F425
Annotation score5
Enzymatic activity
Catalytic site (original residue number in PDB) K233 E259 R260 R435
Catalytic site (residue number reindexed from 1) K155 E181 R182 R357
Enzyme Commision number 7.1.2.2: H(+)-transporting two-sector ATPase.
Gene Ontology
Molecular Function
GO:0005524 ATP binding
GO:0016787 hydrolase activity
GO:0016887 ATP hydrolysis activity
GO:0046933 proton-transporting ATP synthase activity, rotational mechanism
GO:0046961 proton-transporting ATPase activity, rotational mechanism
Biological Process
GO:0006754 ATP biosynthetic process
GO:0015986 proton motive force-driven ATP synthesis
GO:0042776 proton motive force-driven mitochondrial ATP synthesis
GO:0046034 ATP metabolic process
GO:1902600 proton transmembrane transport
Cellular Component
GO:0005739 mitochondrion
GO:0009507 chloroplast
GO:0016020 membrane
GO:0045261 proton-transporting ATP synthase complex, catalytic core F(1)

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Molecular Function
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Biological Process
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Cellular Component
External links
PDB RCSB:6tmk, PDBe:6tmk, PDBj:6tmk
PDBsum6tmk
PubMed33402698
UniProtA0A125YYY4

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